Effect of advanced glycation end products on lens epithelial cells in vitro

The extended exposure of proteins to reducing sugars leads to nonenzymatic glycation with the accumulation of advanced glycation end products (AGEs). Long-lived proteins, such as collagen and crystallins, are subjected to thi s modification, and are implicated as causal factors in several diseases in cluding diabetic complications, cataracts, and arteriosclerosis. One means through which ACEs modulate cellular interactions is via binding to specifi c receptors. In the current study, the existence of AGEs in human anterior polar lens capsules of cataracts was confirmed using a combination of dot-i mmunoblot and fluorescent detection. Human lens epithelial cells (LECs) att ached to anterior lens capsules expressed mRNA for the receptor for AGEs (R AGE). The interaction of LECs with AGEs using bovine lens epithelial explan ts demonstrated that AGEs induced mRNAs and proteins of fibronectin, collag en type I, aberrant extracellular matrix proteins, and (alpha-SMA, a specif ic marker for myofibroblastic cells. These findings suggest that AGEs may a lter cellular functions which induce mRNAs and proteins associated with fib rosis in LECs. (C) 2000 Academic Press.